Dihydrodipicolinate synthase
Class of enzymes
From Wikipedia, the free encyclopedia
4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming).[1][2][3][4] This enzyme catalyses the following chemical reaction
- pyruvate + L-aspartate-4-semialdehyde (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O
| 4-hydroxy-tetrahydrodipicolinate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Dihydrodipicolinate synthase homotetramer, Vitis vinifera | |||||||||
| Identifiers | |||||||||
| EC no. | 4.3.3.7 | ||||||||
| CAS no. | 9055-59-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Dihydrodipicolinate synthetase family | |||||||
|---|---|---|---|---|---|---|---|
 Crystal structure of dihydrodipicolinate synthase dapa-2 (ba3935) from Bacillus anthracis at 1.94a resolution. | |||||||
| Identifiers | |||||||
| Symbol | DHDPS | ||||||
| Pfam | PF00701 | ||||||
| Pfam clan | CL0036 | ||||||
| InterPro | IPR002220 | ||||||
| PROSITE | PDOC00569 | ||||||
| SCOP2 | 1dhp / SCOPe / SUPFAM | ||||||
| CDD | cd00950 | ||||||
| |||||||
The reaction proceeds in three consecutive steps.
Function
This enzyme belongs is a lyase, specifically an amine-lyases, which cleave carbon-nitrogen bonds. 4-Hydroxy-tetrahydrodipicolinate synthase catalyzes lysine biosynthesis via the diaminopimelate pathway of prokaryotes, some phycomycetes, and higher plants. The enzyme catalyses the condensation of L-aspartate-beta-semialdehyde and pyruvate to 4-hydroxy-tetrahydropicolinic acid via a ping-pong mechanism in which pyruvate binds to the enzyme by forming a Schiff base with a lysine residue.[5]
Related enzymes
Three other proteins are structurally related to this enzyme and probably also act via a similar catalytic mechanism. These are Escherichia coli N-acetylneuraminate lyase (EC 4.1.3.3) (protein NanA), which catalyses the condensation of N-acetyl-D-mannosamine and pyruvate to form N-acetylneuraminate; Rhizobium meliloti (Sinorhizobium meliloti) protein MosA,[6] which is involved in the biosynthesis of the rhizopine 3-O-methyl-scyllo-inosamine; and E. coli hypothetical protein YjhH.
Structure
The sequences of 4-hydroxy-tetrahydrodipicolinate synthase from different sources are well-conserved. The structure takes the form of a homotetramer, in which 2 monomers are related by an approximate 2-fold symmetry.[5] Each monomer comprises 2 domains: an 8-fold α/β-barrel, and a C-terminal α-helical domain. The fold resembles that of N-acetylneuraminate lyase. The active site lysine is located in the barrel domain, and has access via 2 channels on the C-terminal side of the barrel.
